An investigation into the nature of the interactions of both large-type (bovine) and small-type (mouse) myelin basic proteins with selected ligands is proposed. The binding of detergents such as sodium dodecyl sulfate, sodium deoxycholate and cetyltrimethylammonium bromide as well as various phospholipids, cerebrosides and sterols to the myelin basic protein will be studied. Ligand binding will be determined by conventional techniques as well as NMR spectroscopy in order to define the nature of the interactions of these detergents and lipids with the protein as well as conformational changes induced upon the protein as a consequence of ligand binding. A comparison of the effects of the binding of these detergents and lipids on the large- and small-type myelin basic proteins will be made.